ID A0A409WWU7_9AGAR Unreviewed; 714 AA.
AC A0A409WWU7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=CVT26_005521 {ECO:0000313|EMBL:PPQ82985.1};
OS Gymnopilus dilepis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Gymnopilus.
OX NCBI_TaxID=231916 {ECO:0000313|EMBL:PPQ82985.1, ECO:0000313|Proteomes:UP000284706};
RN [1] {ECO:0000313|EMBL:PPQ82985.1, ECO:0000313|Proteomes:UP000284706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRW20 {ECO:0000313|EMBL:PPQ82985.1,
RC ECO:0000313|Proteomes:UP000284706};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000256|ARBA:ARBA00001792};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the TPA1 family.
CC {ECO:0000256|ARBA:ARBA00007443}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPQ82985.1}.
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DR EMBL; NHYE01004674; PPQ82985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409WWU7; -.
DR STRING; 231916.A0A409WWU7; -.
DR InParanoid; A0A409WWU7; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000284706; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
DR Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000284706};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 187..304
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 79315 MW; AA72E04378701CBD CRC64;
MARTRERSPS PDAAQSPSSL KKLKTGHVSP SGPQATTVQS PNHLPTPPSD AGSLCPDGPP
SHFADDLFDH NNIARLNADY AENTPFKYAI VEKLFQDDLL KKVKDECLNE LNFTEKETDI
YKVTSAVPRA VLTIPVNQTG DLASLDYLTP TQIARLPNLL ALRDALYSPQ FRKFLRAVTG
CGPLSGKKQD MSVNSYTRGC HLLNHDDVIG TRRVSYILYM PLPHYQLWQK DWGGALELYP
TRINAEGQPE PVNIPSKSIP PSWNQFIFFE VQPGKSFHSV EEVVVGGKGE DGRERLSISG
WFHAAQEGEE GYVPEPPETT EIKSSREQLA STSTVFKSYP THDDVDVLAD VTLSEDHIAF
LSEFLNPVYL QPRTMKALAA RFAEESSLEL HSFLNTPLAE ALEQRLRDLD TRDGLGENRA
GQIPPHTSGT VGASAWTIKG PPHKWRYCVL RSHEDGAPIE AVTPRHASST DQIMRSLQDE
LFASSAFRAW LSIVSRLMPM RYAVEARRFR PGLDYTLATS EESEARLDVV LGLTPPARDP
DSDEEDRFAQ HQRGWTDSDW GGWECYMAPH NEEDDPAIYR SGSSKKSSKP AMNHTTSGES
VASSSTAGPS HSHSNGNGHS TNNNNHHTDN HSSHSHEDDP MNEDNEEEED ESTLLAVQPG
FNRLLLVLRD ERVMRFVKYV SAAAEGSRWD VCGEYEVGII QEDGEDEEEG GRSS
//
